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P20333

- TNR1B_HUMAN

UniProt

P20333 - TNR1B_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 1B

Gene

TNFRSF1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (27 May 2002)
      Previous versions | rss
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    Functioni

    Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. tumor necrosis factor-activated receptor activity Source: ProtInc
    3. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. cellular response to growth factor stimulus Source: Ensembl
    3. cellular response to lipopolysaccharide Source: BHF-UCL
    4. immune response Source: Ensembl
    5. inflammatory response Source: Ensembl
    6. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    7. negative regulation of inflammatory response Source: Ensembl
    8. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
    9. RNA destabilization Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 1B
    Alternative name(s):
    Tumor necrosis factor receptor 2
    Short name:
    TNF-R2
    Tumor necrosis factor receptor type II
    Short name:
    TNF-RII
    Short name:
    TNFR-II
    p75
    p80 TNF-alpha receptor
    CD_antigen: CD120b
    INN: Etanercept
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TNFRSF1B
    Synonyms:TNFBR, TNFR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11917. TNFRSF1B.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane raft Source: BHF-UCL
    4. neuronal cell body Source: Ensembl
    5. nucleus Source: Ensembl
    6. perinuclear region of cytoplasm Source: Ensembl
    7. plasma membrane Source: UniProtKB-SubCell
    8. varicosity Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Pharmaceutical usei

    Available under the name Enbrel (Immunex and Wyeth-Ayerst). Used to treat moderate to severe rheumatoid arthritis (RA). Enbrel consist of the extracellular ligand-binding portion of TNFRSF1B linked to an immunoglobulin Fc chain. It binds to TNF-alpha and blocks its interactions with receptors.

    Organism-specific databases

    PharmGKBiPA36610.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 461439Tumor necrosis factor receptor superfamily member 1b, membrane formPRO_0000034548Add
    BLAST
    Chaini27 – ?Tumor necrosis factor-binding protein 2PRO_0000034549

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 53PROSITE-ProRule annotation
    Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
    Disulfide bondi57 ↔ 75PROSITE-ProRule annotation
    Disulfide bondi78 ↔ 93PROSITE-ProRule annotation
    Disulfide bondi96 ↔ 110PROSITE-ProRule annotation
    Disulfide bondi100 ↔ 118PROSITE-ProRule annotation
    Disulfide bondi120 ↔ 126PROSITE-ProRule annotation
    Disulfide bondi134 ↔ 143PROSITE-ProRule annotation
    Disulfide bondi137 ↔ 161PROSITE-ProRule annotation
    Disulfide bondi164 ↔ 179PROSITE-ProRule annotation
    Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated; mainly on serine residues and with a very low level on threonine residues.
    A soluble form (tumor necrosis factor binding protein 2) is produced from the membrane form by proteolytic processing.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP20333.
    PeptideAtlasiP20333.
    PRIDEiP20333.

    PTM databases

    PhosphoSiteiP20333.

    Miscellaneous databases

    PMAP-CutDBP20333.

    Expressioni

    Gene expression databases

    ArrayExpressiP20333.
    BgeeiP20333.
    CleanExiHS_TNFRSF1B.
    GenevestigatoriP20333.

    Organism-specific databases

    HPAiCAB013045.
    HPA004796.

    Interactioni

    Subunit structurei

    Binds to TRAF2. Interacts with BMX.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRNP287995EBI-358983,EBI-747754
    TNFP013752EBI-358983,EBI-359977
    TRAF2Q129333EBI-358983,EBI-355744

    Protein-protein interaction databases

    BioGridi112987. 26 interactions.
    DIPiDIP-78N.
    IntActiP20333. 12 interactions.
    MINTiMINT-134958.
    STRINGi9606.ENSP00000365435.

    Structurei

    Secondary structure

    1
    461
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 474
    Turni48 – 514
    Beta strandi52 – 554
    Beta strandi61 – 655
    Beta strandi74 – 774
    Beta strandi86 – 883
    Beta strandi104 – 1085
    Beta strandi112 – 1143
    Beta strandi117 – 1204
    Beta strandi124 – 1296
    Beta strandi131 – 1399
    Beta strandi147 – 1515
    Turni154 – 1563
    Beta strandi160 – 1634
    Beta strandi174 – 1763
    Beta strandi194 – 1963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CA9X-ray2.30G/H420-428[»]
    3ALQX-ray3.00R/S/T/U/V/W33-205[»]
    ProteinModelPortaliP20333.
    SMRiP20333. Positions 37-200.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20333.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 257235ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini288 – 461174CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei258 – 28730HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati39 – 7638TNFR-Cys 1Add
    BLAST
    Repeati77 – 11842TNFR-Cys 2Add
    BLAST
    Repeati119 – 16244TNFR-Cys 3Add
    BLAST
    Repeati163 – 20139TNFR-Cys 4Add
    BLAST

    Sequence similaritiesi

    Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG42764.
    HOGENOMiHOG000132845.
    HOVERGENiHBG054237.
    InParanoidiP20333.
    KOiK05141.
    OMAiGNASMDA.
    OrthoDBiEOG786H2Q.
    PhylomeDBiP20333.
    TreeFamiTF331157.

    Family and domain databases

    InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020411. TNFR_1B.
    [Graphical view]
    PfamiPF00020. TNFR_c6. 2 hits.
    [Graphical view]
    PRINTSiPR01919. TNFACTORR1B.
    SMARTiSM00208. TNFR. 4 hits.
    [Graphical view]
    PROSITEiPS00652. TNFR_NGFR_1. 2 hits.
    PS50050. TNFR_NGFR_2. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P20333-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAPVAVWAAL AVGLELWAAA HALPAQVAFT PYAPEPGSTC RLREYYDQTA    50
    QMCCSKCSPG QHAKVFCTKT SDTVCDSCED STYTQLWNWV PECLSCGSRC 100
    SSDQVETQAC TREQNRICTC RPGWYCALSK QEGCRLCAPL RKCRPGFGVA 150
    RPGTETSDVV CKPCAPGTFS NTTSSTDICR PHQICNVVAI PGNASMDAVC 200
    TSTSPTRSMA PGAVHLPQPV STRSQHTQPT PEPSTAPSTS FLLPMGPSPP 250
    AEGSTGDFAL PVGLIVGVTA LGLLIIGVVN CVIMTQVKKK PLCLQREAKV 300
    PHLPADKARG TQGPEQQHLL ITAPSSSSSS LESSASALDR RAPTRNQPQA 350
    PGVEASGAGE ARASTGSSDS SPGGHGTQVN VTCIVNVCSS SDHSSQCSSQ 400
    ASSTMGDTDS SPSESPKDEQ VPFSKEECAF RSQLETPETL LGSTEEKPLP 450
    LGVPDAGMKP S 461
    Length:461
    Mass (Da):48,291
    Last modified:May 27, 2002 - v3
    Checksum:i603D0AE1CD69ACBF
    GO
    Isoform 2 (identifier: P20333-2) [UniParc]FASTAAdd to Basket

    Also known as: DS-TNFR2(Delta7,8), sTNFR2

    The sequence of this isoform differs from the canonical sequence as follows:
         263-268: GLIVGV → ASLACR
         269-461: Missing.

    Show »
    Length:268
    Mass (Da):28,461
    Checksum:i51A97BA5222FA444
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 373EPG → APT AA sequence (PubMed:8015639)Curated
    Sequence conflicti98 – 981S → P in AAN72434. (PubMed:14688072)Curated
    Sequence conflicti102 – 1021S → P in AAN72434. (PubMed:14688072)Curated
    Sequence conflicti141 – 1411R → P in AAA63262. (PubMed:2166946)Curated
    Sequence conflicti363 – 3631A → T in AAA63262. (PubMed:2166946)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti187 – 1871V → M.1 Publication
    Corresponds to variant rs2228494 [ dbSNP | Ensembl ].
    VAR_017176
    Natural varianti196 – 1961M → R Frequent polymorphism; seems to be associated with hyperandrogenism, polycystic ovary syndrome (PCOS) and systemic lupus erythematosus. 7 Publications
    Corresponds to variant rs1061622 [ dbSNP | Ensembl ].
    VAR_015434
    Natural varianti232 – 2321E → K.4 Publications
    Corresponds to variant rs5746026 [ dbSNP | Ensembl ].
    VAR_015435
    Natural varianti236 – 2361A → T.1 Publication
    Corresponds to variant rs5746027 [ dbSNP | Ensembl ].
    VAR_017177
    Natural varianti264 – 2641L → P.1 Publication
    Corresponds to variant rs2229700 [ dbSNP | Ensembl ].
    VAR_017178
    Natural varianti269 – 2691T → P.1 Publication
    Corresponds to variant rs17879042 [ dbSNP | Ensembl ].
    VAR_017179
    Natural varianti295 – 2951Q → R.1 Publication
    Corresponds to variant rs5746032 [ dbSNP | Ensembl ].
    VAR_017180
    Natural varianti301 – 3011P → R.1 Publication
    Corresponds to variant rs17883432 [ dbSNP | Ensembl ].
    VAR_017181

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei263 – 2686GLIVGV → ASLACR in isoform 2. 1 PublicationVSP_011826
    Alternative sequencei269 – 461193Missing in isoform 2. 1 PublicationVSP_011827Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55994 mRNA. Translation: AAA36755.1.
    M32315 mRNA. Translation: AAA59929.1.
    U52165
    , U52156, U52157, U52158, U52159, U52160, U52161, U52162, U52163, U52164 Genomic DNA. Translation: AAC50622.1.
    AY148473 mRNA. Translation: AAN72434.1.
    BT019927 mRNA. Translation: AAV38730.1.
    AY264804 Genomic DNA. Translation: AAO89076.1.
    AY342040 Genomic DNA. Translation: AAP88939.1.
    AL031276, AL357835 Genomic DNA. Translation: CAI19225.1.
    AL357835, AL031276 Genomic DNA. Translation: CAH73721.1.
    CH471130 Genomic DNA. Translation: EAW71733.1.
    BC052977 mRNA. Translation: AAH52977.1.
    S63368 mRNA. Translation: AAB19824.2.
    M35857 mRNA. Translation: AAA63262.1.
    AB030950 Genomic DNA. Translation: BAA89053.1.
    CCDSiCCDS145.1. [P20333-1]
    PIRiA35356.
    RefSeqiNP_001057.1. NM_001066.2. [P20333-1]
    UniGeneiHs.256278.

    Genome annotation databases

    EnsembliENST00000376259; ENSP00000365435; ENSG00000028137. [P20333-1]
    GeneIDi7133.
    KEGGihsa:7133.
    UCSCiuc001att.3. human. [P20333-1]

    Polymorphism databases

    DMDMi21264534.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    NIEHS-SNPs
    Enbrel

    Clinical information on Enbrel

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55994 mRNA. Translation: AAA36755.1 .
    M32315 mRNA. Translation: AAA59929.1 .
    U52165
    , U52156 , U52157 , U52158 , U52159 , U52160 , U52161 , U52162 , U52163 , U52164 Genomic DNA. Translation: AAC50622.1 .
    AY148473 mRNA. Translation: AAN72434.1 .
    BT019927 mRNA. Translation: AAV38730.1 .
    AY264804 Genomic DNA. Translation: AAO89076.1 .
    AY342040 Genomic DNA. Translation: AAP88939.1 .
    AL031276 , AL357835 Genomic DNA. Translation: CAI19225.1 .
    AL357835 , AL031276 Genomic DNA. Translation: CAH73721.1 .
    CH471130 Genomic DNA. Translation: EAW71733.1 .
    BC052977 mRNA. Translation: AAH52977.1 .
    S63368 mRNA. Translation: AAB19824.2 .
    M35857 mRNA. Translation: AAA63262.1 .
    AB030950 Genomic DNA. Translation: BAA89053.1 .
    CCDSi CCDS145.1. [P20333-1 ]
    PIRi A35356.
    RefSeqi NP_001057.1. NM_001066.2. [P20333-1 ]
    UniGenei Hs.256278.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CA9 X-ray 2.30 G/H 420-428 [» ]
    3ALQ X-ray 3.00 R/S/T/U/V/W 33-205 [» ]
    ProteinModelPortali P20333.
    SMRi P20333. Positions 37-200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112987. 26 interactions.
    DIPi DIP-78N.
    IntActi P20333. 12 interactions.
    MINTi MINT-134958.
    STRINGi 9606.ENSP00000365435.

    Chemistry

    ChEMBLi CHEMBL1250356.
    DrugBanki DB00005. Etanercept.
    DB00065. Infliximab.
    GuidetoPHARMACOLOGYi 1871.

    PTM databases

    PhosphoSitei P20333.

    Polymorphism databases

    DMDMi 21264534.

    Proteomic databases

    PaxDbi P20333.
    PeptideAtlasi P20333.
    PRIDEi P20333.

    Protocols and materials databases

    DNASUi 7133.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376259 ; ENSP00000365435 ; ENSG00000028137 . [P20333-1 ]
    GeneIDi 7133.
    KEGGi hsa:7133.
    UCSCi uc001att.3. human. [P20333-1 ]

    Organism-specific databases

    CTDi 7133.
    GeneCardsi GC01P012161.
    HGNCi HGNC:11917. TNFRSF1B.
    HPAi CAB013045.
    HPA004796.
    MIMi 191191. gene.
    neXtProti NX_P20333.
    PharmGKBi PA36610.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42764.
    HOGENOMi HOG000132845.
    HOVERGENi HBG054237.
    InParanoidi P20333.
    KOi K05141.
    OMAi GNASMDA.
    OrthoDBi EOG786H2Q.
    PhylomeDBi P20333.
    TreeFami TF331157.

    Miscellaneous databases

    EvolutionaryTracei P20333.
    GeneWikii TNFRSF1B.
    GenomeRNAii 7133.
    NextBioi 27909.
    PMAP-CutDB P20333.
    PROi P20333.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20333.
    Bgeei P20333.
    CleanExi HS_TNFRSF1B.
    Genevestigatori P20333.

    Family and domain databases

    InterProi IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020411. TNFR_1B.
    [Graphical view ]
    Pfami PF00020. TNFR_c6. 2 hits.
    [Graphical view ]
    PRINTSi PR01919. TNFACTORR1B.
    SMARTi SM00208. TNFR. 4 hits.
    [Graphical view ]
    PROSITEi PS00652. TNFR_NGFR_1. 2 hits.
    PS50050. TNFR_NGFR_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A second tumor necrosis factor receptor gene product can shed a naturally occurring tumor necrosis factor inhibitor."
      Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W., Hale K.K., Squires C.H., Thompson R.C., Vannice J.L.
      Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-196.
    2. "A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins."
      Smith C.A., Davis T., Anderson D., Solam L., Beckmann M.P., Jerzy R., Dower S.K., Cosman D., Goodwin R.G.
      Science 248:1019-1023(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    4. "Identification and characterization of a novel spliced variant that encodes human soluble tumor necrosis factor receptor 2."
      Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D., Ricart W., Engel P.
      Int. Immunol. 16:169-177(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION (ISOFORM 2).
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. NIEHS SNPs program
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-187; ARG-196; LYS-232; THR-236; PRO-264 AND ARG-295.
    7. SeattleSNPs variation discovery resource
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-196; LYS-232; PRO-269 AND ARG-301.
    8. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: PNS.
    11. "Purification and partial amino acid sequence analysis of two distinct tumor necrosis factor receptors from HL60 cells."
      Loetscher H., Schlaeger E.J., Lahm H.-W., Pan Y.-C.E., Lesslauer W., Brockhaus M.
      J. Biol. Chem. 265:20131-20138(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-40; 65-69; 136-141; 300-306 AND 346-362.
    12. "Purification of two types of TNF inhibitors in the urine of the patient with chronic glomerulonephritis."
      Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.
      Nephron 66:386-390(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-37.
      Tissue: Urine.
    13. "Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors."
      Engelmann H., Novick D., Wallach D.
      J. Biol. Chem. 265:1531-1536(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-31.
      Tissue: Urine.
    14. "Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences."
      Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R., Brockhaus M., Lesslauer W.
      Cytokine 2:231-237(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-461 (ISOFORM 1).
    15. "Complementary DNA cloning of a receptor for tumor necrosis factor and demonstration of a shed form of the receptor."
      Heller R.A., Song K., Onasch M.A., Fischer W.H., Chang D., Ringold G.M.
      Proc. Natl. Acad. Sci. U.S.A. 87:6151-6155(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 116-461 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT ARG-196.
    16. "New single nucleotide polymorphisms in the coding region of human TNFR2: association with systemic lupus erythematosus."
      Tsuchiya N., Komata T., Matsushita M., Ohashi J., Tokunaga K.
      Genes Immun. 1:501-503(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-183, VARIANTS ARG-196 AND LYS-232.
    17. "Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation."
      Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M., Lipari M.T., Goeddel D.V.
      J. Biol. Chem. 267:21172-21178(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    18. "A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor."
      Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.
      Cell 78:681-692(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF2.
    19. "Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase: role in endothelial cell migration and angiogenesis."
      Pan S., An P., Zhang R., He X., Yin G., Min W.
      Mol. Cell. Biol. 22:7512-7523(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BMX.
    20. "Structural basis for self-association and receptor recognition of human TRAF2."
      Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.
      Nature 398:533-538(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 419-428 IN COMPLEX WITH TRAF2.
    21. "Association of tumor necrosis factor receptor type II polymorphism 196R with systemic lupus erythematosus in the Japanese: molecular and functional analysis."
      Morita C., Horiuchi T., Tsukamoto H., Hatta N., Kikuchi Y., Arinobu Y., Otsuka T., Sawabe T., Harashima S., Nagasawa K., Niho Y.
      Arthritis Rheum. 44:2819-2827(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARG-196 AND LYS-232.
    22. "Comment: the methionine 196 arginine polymorphism in exon 6 of the TNF receptor 2 gene (TNFRSF1B) is associated with the polycystic ovary syndrome and hyperandrogenism."
      Peral B., San Millan J.L., Castello R., Moghetti P., Escobar-Morreale H.F.
      J. Clin. Endocrinol. Metab. 87:3977-3983(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-196.

    Entry informationi

    Entry nameiTNR1B_HUMAN
    AccessioniPrimary (citable) accession number: P20333
    Secondary accession number(s): B1AJZ3
    , Q16042, Q6YI29, Q9UIH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 171 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3